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The emerging roles of the DDX41 protein in immunity and diseases
Yan Jiang,Yanping Zhu,Zhi-Jie Liu,Songying Ouyang
Protein Cell. 2017, 8 (2 ): 83-89.
https://doi.org/10.1007/s13238-016-0303-4
RNA helicases are involved in almost every aspect of RNA, from transcription to RNA decay. DExD/H-box helicases comprise the largest SF2 helicase superfamily, which are characterized by two conserved RecA-like domains. In recent years, an increasing number of unexpected functions of these proteins have been discovered. They play important roles not only in innate immune response but also in diseases like cancers and chronic hepatitis C. In this review, we summarize the recent literatures on one member of the SF2 superfamily, the DEADbox protein DDX41. After bacterial or viral infection, DNA or cyclic-di-GMP is released to cells. After phosphorylation of Tyr414 by BTK kinase, DDX41 will act as a sensor to recognize the invaders, followed by induction of type I interferons (IFN). After the immune response, DDX41 is degraded by the E3 ligase TRIM21, using Lys9 and Lys115 of DDX41 as the ubiquitination sites. Besides the roles in innate immunity, DDX41 is also related to diseases. An increasing number of both inherited and acquired mutations in DDX41 gene are identified from myelodysplastic syndrome and/or acute myeloid leukemia (MDS/AML) patients. The review focuses on DDX41, as well as its homolog Abstrakt in Drosophila, which is important for survival at all stages throughout the life cycle of the fly.
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Force-dependent calcium signaling and its pathway of human neutrophils on P-selectin in flow
Bing Huang,Yingchen Ling,Jiangguo Lin,Xin Du,Ying Fang,Jianhua Wu
Protein Cell. 2017, 8 (2 ): 103-113.
https://doi.org/10.1007/s13238-016-0364-4
P-selectin engagement of P-selectin glycoprotein ligand-1 (PSGL-1) causes circulating leukocytes to roll on and adhere to the vascular surface, and mediates intracellular calcium flux, a key but unclear event for subsequent arresting firmly at and migrating into the infection or injured tissue. Using a parallel plate flow chamber technique and intracellular calcium ion detector (Fluo-4 AM), the intracellular calciumflux of firmly adhered neutrophils on immobilized P-selectin in the absence of chemokines at various wall shear stresseswas investigated here in real time by fluorescence microscopy. The results demonstrated that P-selectin engagement of PSGL-1 induced the intracellular calcium flux of firmly adhered neutrophils in flow, increasing P-selectin concentration enhanced cellular calcium signaling, and, force triggered, enhanced and quickened the cytoplasmic calcium bursting of neutrophils on immobilized P-selectin. This P-selectin-induced calcium signaling should come from intracellular calcium release rather than extracellular calcium influx, and be along the mechano-chemical signal pathway involving the cytoskeleton, moesin and Spleen tyrosine kinase (Syk). These results provide a novel insight into the mechano-chemical regulation mechanism for P-selectininduced calcium signaling of neutrophils in flow.
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miR-27b inhibits gastric cancer metastasis by targeting NR2F2
Qingzhao Feng,Xionglin Wu,Fuchao Li,Beibei Ning,Xiaofeng Lu,Yin Zhang,Ying Pan,Wenxian Guan
Protein Cell. 2017, 8 (2 ): 114-122.
https://doi.org/10.1007/s13238-016-0340-z
Increasing attention is focused on the down-regulation of miRNAs in cancer process. Nuclear receptor subfamily 2 (NR2F2, also known as COUP-TFII) is involved in the development of many types of cancers, but its role in gastric cancer remains elusive. In this experiment, oncomine and Kaplan-meier database revealed that NR2F2 was up-regulated in gastric cancer and that the high NR2F2 expression contributed to poor survival. MicroRNA-27b was targeted and down-regulated by NR2F2 in human gastric cancer tissues and cells. The ectopic expression of miR-27b inhibited gastric cancer cell proliferation and tumor growth in vitro and in vivo . Assays suggested that the overexpression of miR-27b could promote MGC-803 cells’ migration and invasion and retard their metastasis to the liver. In addition, down-regulation of miR-27b enhanced GES-1 cells’ proliferation and metastasis in vitro . These findings reveal that miR-27b is a tumor suppressor in gastric cancer and a biomarker for improving patients’ survival.
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Mass spectrometry based proteomics profiling of human monocytes
Yong Zeng,Fei-Yan Deng,Wei Zhu,Lan Zhang,Hao He,Chao Xu,Qing Tian,Ji-Gang Zhang,Li-Shu Zhang,Hong-Gang Hu,Hong-Wen Deng
Protein Cell. 2017, 8 (2 ): 123-133.
https://doi.org/10.1007/s13238-016-0342-x
Human monocyte is an important cell type which is involved in various complex human diseases. To better understand the biology of human monocytes and facilitate further studies, we developed the first comprehensive proteome knowledge base specifically for human monocytes by integrating both in vivo and in vitro datasets. The top 2000 expressed genes from in vitro datasets and 779 genes from in vivo experiments were integrated into this study. Altogether, a total of 2237 unique monocyte-expressed genes were cataloged. Biological functions of these monocyte-expressed genes were annotated and classified via Gene Ontology (GO) analysis. Furthermore, by extracting the overlapped genes from in vivo and in vitro datasets, a core gene list including 541 unique genes was generated. Based on the core gene list, further gene-disease associations, pathway and network analyses were performed. Data analyses based on multiple bioinformatics tools produced a large body of biologically meaningful information, and revealed a number of genes such as SAMHD1 , G6PD , GPD2 and ENO1 , which have been reported to be related to immune response, blood biology, bone remodeling, and cancer respectively. As a unique resource, this study can serve as a reference map for future in-depth research on monocytes biology and monocyte-involved human diseases.
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Protein-protein interaction analysis in crude bacterial lysates using combinational method of 19 F site-specific incorporation and 19 F NMR
Dong Li,Yanan Zhang,Yao He,Chengwei Zhang,Jiefei Wang,Ying Xiong,Longhua Zhang,Yangzhong Liu,Pan Shi,Changlin Tian
Protein Cell. 2017, 8 (2 ): 149-154.
https://doi.org/10.1007/s13238-016-0336-8
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